EC Number   |
Recommended Name  |
Application |
|---|
    1.1.1.198 | (+)-borneol dehydrogenase |
synthesis |
production of enzyme in the form of inclusion body in Escherichia coli. The refolded BDH1 tends to precipitate. Insoluble recombinant BDH1 is converted into a soluble form by adding glycerol in LB medium |
| 1.1.1.198 | (+)-borneol dehydrogenase |
synthesis |
recombinant borneol dehydrogenase is found in inclusion bodies when expressed in Escherichia coli. Changing the medium from lysogeny broth to Terrific Broth yield a soluble form of the enzyme |
| 4.2.3.13 | (+)-delta-cadinene synthase |
synthesis |
expression in Saccharomyces cerevisiae leads to a titer of (-)-alpha-copaene of 9 mg/l at 48 h and around 7 mg/l in Escherichia coli, and the titer of (+)-delta-cadinene is 6 mg/l in Saccharomyces cerevisiae and 3.5 mg/l in Escherichia coli |
| 3.5.2.B2 | (+)-gamma-lactamase |
synthesis |
enantioselective resolution of 100 g/l 2-azabicyclo[2.2.1]hept-5-en-3-one, is achieved with 10 g/l dry cells, resulting in 55.2% conversion and 99% enantiomeric excess of the (-)-gamma-lactam, i.e. (1R,4S)-2-azabicyclo[2.2.1]hept-5-en-3-one |
| 3.5.2.B2 | (+)-gamma-lactamase |
synthesis |
the enantiomers of substrate 2-azabicyclo[2.2.1]hept-5-en-3-one (gamma-lactam) are key chiral synthons in the synthesis of antiviral drugs such as carbovir and abacavir |
| 3.5.2.B2 | (+)-gamma-lactamase |
synthesis |
(+)-gamma-lactamase catalyzes the specific hydrolysis of (+)-gamma-lactam out of the racemic gamma-lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) to leave optically pure (-)-gamma-lactam, which is the key building block of antiviral drugs such as carbovir and abacavir |
| 3.5.2.B2 | (+)-gamma-lactamase |
synthesis |
mutant enzyme Q192S/L223Y can be employed for the preparation of (-)-gamma-lactam and also for that of (2S,3R)-ethyl 3-phenylglycidate |
| 3.5.2.B2 | (+)-gamma-lactamase |
synthesis |
the enzyme may become a potential tool for the production of (-)-gamma-lactam because of its superior physicochemical properties and high enzyme activity |
| 3.5.2.B2 | (+)-gamma-lactamase |
synthesis |
the transformation of an active but unstable mesophilic enzyme into a stable catalyst, achieved by immobilizing the enzyme on macroporous resins, provides a feasible approach for the preparation of optically active (-)-Vince lactam (i.e. 2-azabicyclo [2.2.1] hept-5-en-3-one), which is an important chiral synthon used as an intermediate in organic chemistry |
| 4.2.3.77 | (+)-germacrene D synthase |
synthesis |
improved conditions for expression of Zingiber officinale (+)-germacrene synthase in Escherichia coli. Comparison of bacterial strains; BL21 (DE3), BL21 (DE3) Tuner BL21(DE3) pLysS and BL21 (DE3) pLysS Tuner using different inducing agents. The change between BL21 (DE3) cells and BL21 (DE3) Tuner, induced with IPTG, leads to a twofold increase in enzyme activity in the soluble fraction while a reduction in activity is observed when using the pLysS strains. The same doubling of activity is observed for germacrene synthase when the commonly used BL.21 (DE3) is induced with The Inducer. Addition of 2.5 mM glycine betaine and 660 mM sorbitol to the bacterial growth media results in reduction of growth rate and biomass yield but under these conditions the best overall protein production is obtained |
| 1.1.1.208 | (+)-neomenthol dehydrogenase |
synthesis |
the enzyme is useful, together with menthone:(-)-menthol reductase (EC 1.1.1.207), for production of (1R,2S,5R)-(?)-menthol and (1S,2S,5R)-(+)-neomenthol from pulegone, development of a one-pot synthesis method, overview. Menthol isomers, (1R,2S,5R)-(?)-menthol, (1R,2S,5S)-(+)-isomenthol, (1S,2S,5R)-(+)-neomenthol, and (1R,2R,5R)-(+)-neoisomenthol, and carvone are used as additives in oral hygiene products and flavors in food and beverages, or cosmetics |
| 1.14.14.132 | (-)-4'-demethyl-deoxypodophyllotoxin 4-hydroxylase |
synthesis |
recombinant coexpression of the genes involved in the podophyllotoxin pathway permits to reconstitute the pathway to (-)-4'-demethylepipodophyllotoxin (the etoposide aglycone), a naturally occurring lignan that is the immediate precursor of etoposide and, unlike podophyllotoxin, a potent topoisomerase inhibitor, for production of the etoposide aglycone in tobacco and circumvent the need for cultivation of mayapple and semisynthetic epimerization and demethylation of podophyllotoxin |
| 4.2.3.95 | (-)-alpha-cuprenene synthase |
synthesis |
expression in Xanthophyllomyces dendrorhous leads to production of alpha-cuprenene up to 80 mg/l. At this expression levels the pool of terpene precursors is not a limiting factor since the expression of the Cop6 gene in the genomic rDNA of the yeast allows production of both alpha-cuprenene and astaxanthin without affecting the growth or the accumulation levels of both compounds |
| 4.2.3.119 | (-)-alpha-pinene synthase |
synthesis |
co-expression with over-expressed native 1-deoxy-D-xylulose-5-phosphate synthase and isopentenyl diphosphate isomerase from Corynebacterium glutamicum plus geranyl diphosphate synthase from Abies grandis leads to synthesis of up to 27 microg alpha-pinene per g cell weight |
| 1.1.1.227 | (-)-borneol dehydrogenase |
synthesis |
production of enzyme in the form of inclusion body in Escherichia coli. The refolded BDH1 tends to precipitate. Insoluble recombinant BDH1 is converted into a soluble form by adding glycerol in LB medium |
| 1.14.20.8 | (-)-deoxypodophyllotoxin synthase |
synthesis |
recombinant coexpression of the genes involved in the podophyllotoxin pathway permits to reconstitute the pathway to (-)-4'-demethylepipodophyllotoxin (the etoposide aglycone), a naturally occurring lignan that is the immediate precursor of etoposide and, unlike podophyllotoxin, a potent topoisomerase inhibitor, for production of the etoposide aglycone in tobacco and circumvent the need for cultivation of mayapple and semisynthetic epimerization and demethylation of podophyllotoxin |
| 3.5.2.B3 | (-)-gamma-lactamase |
synthesis |
Mhg can be utilized to prepare chiral gamma-lactam, which is an important chiral intermediate for the synthesis of a series of antiviral drugs, such as abacavir (targeting HIV) and peramivir (targeting hepatitis and pandemic influenza viruses) |
| 3.5.2.B3 | (-)-gamma-lactamase |
synthesis |
(+)-gamma-lactamase catalyzes the specific hydrolysis of (+)-gamma-lactam out of the racemic gamma-lactam (2-azabicyclo[2.2.1]hept-5-en-3-one) to leave optically pure (-)-gamma-lactam, which is the key building block of antiviral drugs such as carbovir and abacavir |
| 3.5.2.B3 | (-)-gamma-lactamase |
synthesis |
bioprocess catalysed by the enzyme is a promising route for the green manufacture of chiral (+)-gamma-lactam |
| 1.1.1.207 | (-)-menthol dehydrogenase |
synthesis |
the enzyme is useful, together with menthone:(+)-neomenthol reductase (EC 1.1.1.208), for production of (1R,2S,5R)-(-)-menthol and (1S,2S,5R)-(+)-neomenthol from pulegone, development of a one-pot synthesis method, overview. Menthol isomers, (1R,2S,5R)-(-)-menthol, (1R,2S,5S)-(+)-isomenthol, (1S,2S,5R)-(+)-neomenthol, and (1R,2R,5R)-(+)-neoisomenthol, and carvone are used as additives in oral hygiene products and flavors in food and beverages, or cosmetics |
| 5.4.99.15 | (1->4)-alpha-D-glucan 1-alpha-D-glucosylmutase |
synthesis |
overexpression of the enzyme treY gene and the treY/treZ synthetic operon encoding enzyme and maltooligosyltrehalose trehalohydrolase significantly increases maltooligosyltrehalose synthase activity, the rate-limiting step, and improves the specific productivity and the final titer of trehalose. Furthermore, a strong decrease is noted in glycogen accumulation. Expression of UDP-glucose pyrophosphorylase/maltooligosyltrehalose synthase and UDP-glucose pyrophosphorylase/maltooligosyltrehalose synthase/maltooligosyltrehalose trehalohydrolase synthetic operons shows a partial recovery in the intracellular glycogen levels and a significant improvement in both intra- and extracellular trehalose content |
| 5.4.99.15 | (1->4)-alpha-D-glucan 1-alpha-D-glucosylmutase |
synthesis |
production of trehalose by enzyme plus maltooligosyltrehalose trehalohydrolase is increased in presence of 4-alpha-glucanotransferase, converting 70% of maltopentaose into trehalose after 6 h, while 60% is converted without 4-alpha-glucanotransferase |
| 5.4.99.15 | (1->4)-alpha-D-glucan 1-alpha-D-glucosylmutase |
synthesis |
conditions for the production of trehalose from starch by thermostable maltooligosyl trehalose synthase and maltooligosyl trehalose trehalohydrolase from Sulfolubus acidocaldarius ATCC 33909 |
| 5.4.99.15 | (1->4)-alpha-D-glucan 1-alpha-D-glucosylmutase |
synthesis |
trehalose production from starch |
| 2.3.1.285 | (13S,14R)-1,13-dihydroxy-N-methylcanadine 13-O-acetyltransferase |
synthesis |
de novo production of noscapine in Saccharomyces cerevisiae, through the reconstruction of a biosynthetic pathway comprising over 30 enzymes from plants, bacteria, mammals, and yeast itself. Optimization of conditions leads to an over 18,000fold improvement from initial noscapine titers to about2.2 mg/l. By feeding modified tyrosine derivatives to the optimized noscapine-producing strain, microbial production of halogenated benzylisoquinoline alkaloids is possible |
| 1.1.1.423 | (1R,2S)-ephedrine 1-dehydrogenase |
synthesis |
the wide substrate spectrum of these dehydrogenases, combined with their regio- and enantioselectivity, suggests a high potential for the industrial production of valuable chiral compounds |
| 1.1.1.423 | (1R,2S)-ephedrine 1-dehydrogenase |
synthesis |
the enzyme catalyzes the oxidation of an isomer of ephedrine and the regio- and enantioselective reduction of sterically demanding substrate 1-phenyl-1,2-propanedione to give (R)-phenylacetylcarbinol |
| 3.1.1.117 | (4-O-methyl)-D-glucuronate---lignin esterase |
synthesis |
due to its thermostability, enzyme CkXyn10C-GE15A is a promising candidate for industrial processes, with both catalytic domains exhibiting melting temperatures over 70°C. Of particular interest is the glucuronoyl esterase domain, as it represents the first studied thermostable enzyme displaying this activity |
| 3.1.1.117 | (4-O-methyl)-D-glucuronate---lignin esterase |
synthesis |
Thermothielavioides terrestris glucoronoyl esterases TtGEs can be used as promising accessory enzymes to improve the hydrolysis efficiency of commercial enzymes in saccharification of lignocellulosic materials due to their thermophilic characteristics |
| 4.1.3.42 | (4S)-4-hydroxy-2-oxoglutarate aldolase |
synthesis |
preparation of (4S)-4-hydroxy-2-oxoglutarate at more than 95% enantiomeric excess by stereospecific synthesis from glyoxylate and pyruvate. Preparation of (4R)-4-hydroxy-2-oxoglutarate at 60% enantiomeric excess by selective cleavage of the (4S)-isomer of racemic 4-hydroxy-2-oxoglutarate leaving the (4R)-isomer in solution |
| 4.2.3.16 | (4S)-limonene synthase |
synthesis |
engineering of Echerichia coli with a heterologous mevalonate pathway and limonene synthase for production of limonene followed by coupling with a cytochrome P450,which specifically hydroxylates limonene to produce perillyl alcohol. A strain containing all mevalonate pathway genes in a single plasmid produces limonene at titers over 400 mg/l from glucose. Incorporation of a cytochrome P450 to hydroxylate limonene yields approximately 100mg/l of perilyl alcohol |
| 6.3.3.4 | (carboxyethyl)arginine beta-lactam-synthase |
synthesis |
clavulanic acid intermediates: deoxygaunidinoproclavaminic acid, guanidinoproclavaminic acid, and dihydroclavaminic acid are heterologously produced in Streptomyces venezuelae recombinant using four sets of early genes from the clavulanic acid biosynthetic pathway |
| 5.4.4.1 | (hydroxyamino)benzene mutase |
synthesis |
expression of enzyme plus nitrobenzene nitroreductase in Escherichia coli. Rapid and stoichiometric conversion of nitrobenzene to 2-aminophenol, of 2-nitroacetophenone to 2-amino-3-hydroxyacetophenone, and of 3-nitroacetophenone to 3-amino-2-hydroxyacetophenone, as well as further conversions. Final yields of aminophenols after extraction and recovery are over 64% |
| 1.2.3.15 | (methyl)glyoxal oxidase |
synthesis |
efficient expression in Pichia pastoris and Trichoderma reesei with subsequent purification by anion exchange and hydrophobic interaction chromatography. Both processes are suitable for the production of the target protein at high levels. GLOX produced in T. reesei carries mainly Man5 glycosylation while the enzyme produced in P. pastoris exhibits the typical high-mannose type N-glycosylation. The enzyme expressed in P. pastoris shows slightly higher specific activities which correlates with the higher copper loading of 65.5 % compared to 51.9 % for the protein from T. reesei |
| 2.4.1.92 | (N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase |
synthesis |
expression of enzyme both as complete membrane-bound enzyme and as a soluble form in the baculovirus insect cell expression system |
| 2.4.1.92 | (N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase |
synthesis |
stable expression of enzyme in CHO-Lec8 cells, production of complex-type N-glycans quantitatively bearing LacdiNAc-structures on their antennae and containing repeating LacdiNAc-structures |
| 2.4.1.92 | (N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase |
synthesis |
the immobilized enzyme might be useful in chemoenzymatical ceramide glycoconjugate synthesis |
| 3.5.1.100 | (R)-amidase |
synthesis |
R-amidase is the first enzyme useful for the enzymatic optical resolution of racemic piperazine-2-tert-butylcarboxamide carried out under mild conditions. Enantiomerically pure piperazine-2-carboxylic acid and its tert-butylcarboxamide derivative are important chiral building blocks for some pharmacologically active compounds such as N-methyl-D-aspartate antagonist for glutamate receptor, cardioprotective nucleoside transport blocker, and HIV protease inhibitor |
| 3.5.1.100 | (R)-amidase |
synthesis |
expression of amidase in Escherichia coli using a T7 promoter. Amidase activity of the engineered Escherichia coli strain reaches 2963 U/l in a 5-l bioreactor, and can be further increased to 5255 U/l in a 100-l bioreactor. Using cell-free extract prepared from 1 kg (wet cell weight) of recombinant cells as catalyst, 60 kg of R,S-DMCPCA is resolved into S-DMCPCA (28.6 kg) and R-2,2-dimethylcyclopropanecarboxylic acid (31.7 kg) in 18 h, and the enantiomeric excess (ee) value of S-DMCPCA reaches 99.32%. 20.5 kg of pure S-DMCPCA is obtained after concentration and crystallization, corresponding to a total yield of 34.2% from R,S-DMCPCA |
| 2.6.1.B21 | (R)-amine:2-oxo acid transaminase |
synthesis |
amine transaminase (ATA) catalyzing stereoselective amination of prochiral ketones is an attractive alternative to transition metal catalysis |
| 2.6.1.B21 | (R)-amine:2-oxo acid transaminase |
synthesis |
development of a one-pot, trienzymatic cascade comprising an (R)-specific omega-transaminase, an amine dehydrogenase, and a formate dehydrogenase for the economical and ecofriendly synthesis of (R)-chiral amines. Using inexpensive ammonium formate as the sole sacrificial agent, the established cascade system enables efficient omega-transaminase-mediated (R)-amination of various ketones, with high conversions and excellent enantiomeric excess (over 99%), water and CO2 are the only waste products |
| 2.6.1.B21 | (R)-amine:2-oxo acid transaminase |
synthesis |
in another reaction for deracemization using enantiocomplementary transaminases, the oxidative deamination step is carried out by alpha-transaminase such as branched-chain transaminase (EC 2.6.1.42) and D-amino acid transaminase (EC 2.6.1.21). It is notable that substitution of alpha-transaminase with alanine dehydrogenase in the deracemization method for production of D-amino acids using L-alanine dehydrogenase (AlaDH), D-selective omega-transaminase (omega-TA) ARTAmut, and NADH oxidase (NOX) eliminates the need for an expensive 2-oxoacid cosubstrate. Feasibility of the stereoinversion reaction is dependent on enzyme activities of AlaDH and onega-TA for L-amino acids and its keto acids, respectively. ARTAmut substrate specificity allows various oxoacids as substrates |
| 2.6.1.B21 | (R)-amine:2-oxo acid transaminase |
synthesis |
pyridoxal-5'-phosphate (PLP)-dependent transaminases are industrially important enzymes catalyzing the stereoselective amination of ketones and keto acids. Transaminases of PLP fold type IV are characterized by (R)- or (S)-stereoselective transfer of amino groups, depending on the substrate profile of the enzyme |
| 2.3.3.21 | (R)-citramalate synthase |
synthesis |
the autrotrophic micro-organism may be engineered for robust butanol and propanol production from 2-ketobutyrate, which is an intermediate in the isoleucine biosynthesis pathway |
| 2.3.3.21 | (R)-citramalate synthase |
synthesis |
synthesis of citramalate at high yield by Escherichia coli overexpressing citramalate synthase. Citramalate is a chemical precursor to the industrially important methacrylic acid. Acetate is an undesirable by-product potentially formed from pyruvate and acetyl-CoA, the precursors of citramalate during aerobic growth of Escherichia coli. Gene deletions critical to reducing acetate accumulation during aerobic growth and citramalate production are ifdentified in metabolically engineered Escherichia coli strains. The key knockouts critical to minimizing acetate formation are identified as pta, ackA and poxB |
| 2.3.3.21 | (R)-citramalate synthase |
synthesis |
synthesis of citramalic acid from glycerol by metabolically engineered Escherichia coli |
| 2.3.3.21 | (R)-citramalate synthase |
synthesis |
in a fedbatch process an exponential feeding strategy using expression of CimA and the citrate synthase GltA F383M variant, over 60 g/l citramalate with a yield of 0.53 g citramalate/g glucose are generated in 132 hr |
| 1.1.1.379 | (R)-mandelate dehydrogenase |
synthesis |
D-mandelate dehydrogenase (DMDH) has the potential to convert D-mandelic acid to phenylglyoxylic acid (PGA), which is a key building block in the field of chemical synthesis and is widely used to synthesize pharmaceutical intermediates or food additives. Development of an alternative strategy for the chiral resolution of racemic mandelic acid and the biosynthesis of PGA |
| 4.1.2.10 | (R)-mandelonitrile lyase |
synthesis |
used as a catalyst in the preparation of optically active cyanohydrins |
| 4.1.2.10 | (R)-mandelonitrile lyase |
synthesis |
(R)-oxynitrilase immobilized as a cross-linked enzyme aggregate via precipitation with 1,2-dimethoxyethane and subsequent cross-linking using glutaraldehyde is stable and recyclable. Application in microaqueous medium, superior biocatalyst for the enantioselective hydrocyanation of slow-reacting aldehydes |
| 4.1.2.10 | (R)-mandelonitrile lyase |
synthesis |
development and validation of a process model for production of (R)-cyanohydrins in an aqueous-organic biphasic-stirred tank reactor with an unknown interfacial area operated in batch mode. The formation of (R)-mandelonitrile from benzaldehyde and cyanide catalyzed by Prunus amygdalus hydroxynitrile lyase is chosen as a model reaction. Methyl tert-butyl ether is selected as the organic solvent and the reaction conditions are 5°C and pH 5.5 at which the nonenzymatic reaction towards rac-mandelonitrile is largely suppressed |
| 4.1.2.10 | (R)-mandelonitrile lyase |
synthesis |
hydroxynitrile lyases are proficient biocatalysts for the stereospecific synthesis of cyanohydrins |
| 4.1.2.10 | (R)-mandelonitrile lyase |
synthesis |
optically active cyanohydrins are expedient starting materials for preparation of alpha-hydroxyketones, alpha-hydroxy acids, beta-aminoalcohols, aminonitriles and aziridines |
| 4.1.2.10 | (R)-mandelonitrile lyase |
synthesis |
optically active cyanoydrins are expedient starting materials for preparation of alpha-hydroxyketones, alpha-hydroxy acids, beta-aminoalcohols, aminonitriles and aziridines |
| 4.1.2.10 | (R)-mandelonitrile lyase |
synthesis |
production of (R)-hydroxypivalaldehyde cyanohydrin, the chiral key precursor in hydroxynitrile lyase based (R)-pantlactone synthesis |
| 4.1.2.10 | (R)-mandelonitrile lyase |
synthesis |
the enantiospecific formation of alpha-hydroxynitriles |
| 4.1.2.10 | (R)-mandelonitrile lyase |
synthesis |
fusion of enzyme to different fluorescent reporter proteins. Flavin-based fluorescent reporter fusions convert 95% benzaldehyde to (R)-mandelonitrile within 60 min at pH 4.75, with 96% enantiomeric excess |
| 4.1.2.10 | (R)-mandelonitrile lyase |
synthesis |
purification of enzyme as crosslinked enzyme aggregates and application for synthesis of enantiopure cyanohydrins |
| 4.1.2.10 | (R)-mandelonitrile lyase |
synthesis |
synthesis of (R)-beta-nitro alcohols using nitromethane as donor. Highest enantioselectivity is obtained with n-butyl acetate as solvent with an optimum aqueous phase content of 50% (v/v) |
| 4.1.2.10 | (R)-mandelonitrile lyase |
synthesis |
Amygdalus pedunculata hydroxynitrile lyase is an excellent biocatalyst and has very high potential for synthesis of enantiopure cyanohydrins |
| 4.1.2.10 | (R)-mandelonitrile lyase |
synthesis |
an easy one-step immobilization of a complex Arabidopsis thaliana hydroxynitrile lyase fusion protein is possible starting from an Escherichia coli crude cell extract (producing a carbohydrate-binding module-containing fusion protein) and cost efficient cellulosic carrier materials. Highly-specific site-selective immobilization of the target protein is achieved by fusing the family 2 carbohydrate-binding module of the exoglucanase/xylanase Cex from Cellulomonas fimi to the target enzyme. This yields a cheap, active, stable and recyclable immobilizate, which can be employed in micro-aqueous reaction systems to enable enantiopure cyanohydrin synthesis |
| 4.1.2.10 | (R)-mandelonitrile lyase |
synthesis |
hydroxynitrile lyases are involved in the synthesis of enantiomerically pure cyanohydrins which are important intermediates in the production of pharmaceuticals and agrochemicals. The enzyme synthesizes (R)-mandelonitrile in both, batch reaction and fed-batch reaction and can be effectively used in the synthesis of (R)-mandelonitrile |
| 4.1.2.10 | (R)-mandelonitrile lyase |
synthesis |
the enzyme has very high potential for synthesis of cyanohydrins and can be used for the production of enantiopure cyanohydrins. Cyanohydrins are important intermediates in the production of pharmaceuticals and agrochemicals |
| 4.1.2.10 | (R)-mandelonitrile lyase |
synthesis |
the enzyme is a powerful and cheap biocatalyst in the synthesis of (R)-mandelonitrile and may be used in combination with nitrilases to produce enantiopure mandelic acids |
| 4.1.2.10 | (R)-mandelonitrile lyase |
synthesis |
the enzyme may find application as a biocatalyst for the synthesis of enantiomerically pure cyanohydrins. DtHNL1-CLEA preparation results in a more robust biocatalyst under acidic conditions, which is an interesting feature for the efficient production of enantiomerically pure cyanohydrins |
| 4.1.2.10 | (R)-mandelonitrile lyase |
synthesis |
the high specific activity toward benzaldehyde along with wide temperature, pH stabilities and high enantioselectivity in the synthesis of various cyanohydrins make this enzyme suitable as an industrial biocatalyst |
| 4.1.2.10 | (R)-mandelonitrile lyase |
synthesis |
the immobilization of partially purified hydroxynitrile lyase from Prunus dulcis as crosslinked enzyme aggregate is a very promising tool owing to its ease of preparation, cheapness, and efficiency in the preparation of enantiopure cyanohydrins. Response surface methodology provides an effective way for the optimization of the preparation of PdHNL-crosslinked enzyme aggregate. The synthesis of (R)-mandelonitrile, (R)-2-chloromandelonitrile, (R)-3,4-dihydroxymandelonitrile, (R)-2-hydroxy-4-phenyl butyronitrile, (R)-4-bromomandelonitrile, (R)-4-fluoromandelonitrile, and (R)-4-nitromandelonitrile is achieved with high yield and enantiomeric excess |
| 1.1.1.B4 | (R)-specific secondary alcohol dehydrogenase (NADH) |
synthesis |
the enzym is useful in production of chiral compounds for organic synthesis |
| 1.1.1.B4 | (R)-specific secondary alcohol dehydrogenase (NADH) |
synthesis |
the enzyme can be used for stereospecific interconversion of (R)-1-phenylethanol and (S)-1-phenylethanol via the oxoform together with the (S)-specific secondary alcohol dehydrogenase using whole cells as biocatalysts that include the required cofactor regenration system, method, overview. Optically pure secondary alcohols are widely used in pharmaceuticals, flavors, agricultural chemicals and specialty materials |
| 1.1.1.B4 | (R)-specific secondary alcohol dehydrogenase (NADH) |
synthesis |
ethyl benzoylformate is asymmetrically reduced by the purified enzyme, using an additional coupled NADH regeneration system, with 95% conversion and in an enantiomeric excess of 99.9% |
| 1.1.1.B4 | (R)-specific secondary alcohol dehydrogenase (NADH) |
synthesis |
using recombinant Escherichia coli cells expressing Sdr, a yield of 82.5% for (R)-[3,5-bis(trifluoromethyl)phenyl]ethanol can be achieved within 12 h at a substrate concentration of up to 1000 M |
| 1.1.1.B4 | (R)-specific secondary alcohol dehydrogenase (NADH) |
synthesis |
the enzyme is coupled with formate dehydrogenase and co-immobilized on SiO2 particles, the system is used for continuous catalytic conversion of beta-hydroxyacetophenone to optically pure (r)-phenylethanediol with in situ NADH regeneration and recycling. Reusable system, method overview |
| 1.1.1.B4 | (R)-specific secondary alcohol dehydrogenase (NADH) |
synthesis |
the enzyme might be useful in application as a replacement of chemical synthesis of aromatic chiral beta-amino alcohols |
| 3.1.6.19 | (R)-specific secondary-alkylsulfatase (type III) |
synthesis |
stereoselctive organic synthesis, stereoselective and enantioselective biohydrolysis of sulfate esters of sec-alcohols |
| 3.1.6.19 | (R)-specific secondary-alkylsulfatase (type III) |
synthesis |
stereoselective organic synthesis, enantioselective hydrolysis of rac-secondary-alkyl sulphate esters |
| 1.1.1.4 | (R,R)-butanediol dehydrogenase |
synthesis |
increase in production of (R,R)-butanediol from xylose in batch and continuous cultures by increase of temperature from 30 to 39°C, analysis of byproducts |
| 1.1.1.4 | (R,R)-butanediol dehydrogenase |
synthesis |
the enzyme is useful in production of 2,3-butanediol, an important starting material for the manufacture of bulk chemicals such as methyl ethyl ketone and 1,3-butadiene |
| 1.1.1.4 | (R,R)-butanediol dehydrogenase |
synthesis |
Paenibacillus brasilensis produces 2,3-butanediol (2,3-BDO) and can be utilized for large scale production |
| 1.1.1.4 | (R,R)-butanediol dehydrogenase |
synthesis |
two coexpressed enantiocomplementary carbonyl reductases, BDHA (2, 3-butanediol dehydrogenase from Bacillus subtilis) and GoSCR (polyol dehydrogenase from Gluconobacter oxydans) are used for asymmetric reduction of 2-hydroxyacetophenone (2-HAP) to (R)-1-phenyl-1,2-ethanediol ((R)-PED) or (S)-1-phenyl-1,2-ethanediol ((S)-PED) with excellent stereochemical selectivity and coupled with cofactor regeneration by GDH. Enantiomerically pure (R)-1-phenyl-1,2-ethanediol ((R)-PED) can be used as a building block for the preparation of (R)-norfluoxetine, (R)-fluoxetine, and beta-lactam antibiotics |
| 2.1.1.115 | (RS)-1-benzyl-1,2,3,4-tetrahydroisoquinoline N-methyltransferase |
synthesis |
the enzyme immobilized on CH-Sepharose or CPG-10 glass beads is a useful tool for the preparative synthesis of isotopically labelled N-methylated benzylisoquinoline alkaloids |
| 2.1.1.128 | (RS)-norcoclaurine 6-O-methyltransferase |
synthesis |
production of the economically important analgesic morphine and the antimicrobial agent berberine |
| 1.14.14.163 | (S)-1-hydroxy-N-methylcanadine 13-hydroxylase |
synthesis |
de novo production of noscapine in Saccharomyces cerevisiae, through the reconstruction of a biosynthetic pathway comprising over 30 enzymes from plants, bacteria, mammals, and yeast itself, including 7 plant endoplasmic reticulum (ER)-localized enzymes. Optimization directed to tuning expression of pathway enzymes, host endogenous metabolic pathways, and fermentation conditions led to an over 18,000-fold improvement from initial noscapine titers to 2.2 mg/l |
| 1.14.14.163 | (S)-1-hydroxy-N-methylcanadine 13-hydroxylase |
synthesis |
reconstitution of the noscapine gene cluster in Saccharomyces cerevisiae to achieve the microbial production of noscapine and related pathway intermediates |
| 1.1.1.311 | (S)-1-phenylethanol dehydrogenase |
synthesis |
application of (S)-1-phenylethanol dehydrogenase for asymmetric reduction of 42 prochiral ketones and 11 beta-keto esters to enantiopure secondary alcohols. The conversions are carried out in a batch reactor using recombinant Escherichia coli as whole-cell catalysts and isopropanol as reaction solvent and cosubstrate for NADH recovery. Ketones are converted to the respective secondary alcohols with excellent enantiomeric excesses and high productivities |
| 1.1.1.311 | (S)-1-phenylethanol dehydrogenase |
synthesis |
the enzyme recombinantly expressed in Escherichia coli is used for chemoenzymatic synthesis of enantiomerically enriched (S)- and (R)-gamma-aryl-gamma-butyrolactones, whereby the key step is an enzyme-catalyzed stereoselective reduction of methyl 4-oxo-4-arylbutanoates, (S)-PED-catalyzed bioreduction in preparative scale |
| 3.8.1.2 | (S)-2-haloacid dehalogenase |
synthesis |
production of D-lactate in industry |
| 3.8.1.2 | (S)-2-haloacid dehalogenase |
synthesis |
production of optically active 2-hydroxyalkanoic acids and 2-haloalkanoic acids for chiral synthesis in industry |
| 3.8.1.2 | (S)-2-haloacid dehalogenase |
synthesis |
His-tagged L-2-haloacid dehalogenase subtype immobilized for production of D-lactate and D-chloropropionic acid |
| 3.8.1.2 | (S)-2-haloacid dehalogenase |
synthesis |
L-2-haloacid dehalogenase subtype produces D-2-hydroxyalkanoic acids for chiral synthesis in industry in water and organic solvents |
| 3.8.1.2 | (S)-2-haloacid dehalogenase |
synthesis |
production of (S)-2-chloropropionic acid, which is used in the synthesis of optically active phenoxypropionic acid herbicides |
| 1.1.3.15 | (S)-2-hydroxy-acid oxidase |
synthesis |
- |
| 1.1.3.15 | (S)-2-hydroxy-acid oxidase |
synthesis |
production of glyoxylate in biocatalysis of co-produced glycolate oxidase and catalase T |
| 1.1.3.15 | (S)-2-hydroxy-acid oxidase |
synthesis |
optimization of enzyme expression in Escherichia coli for production glyoxylate in culture medium |
| 1.1.3.15 | (S)-2-hydroxy-acid oxidase |
synthesis |
optimization of production of lactate oxidase by cultivating strains under high aeration in a medium with 0.5% glucose and 2% lactate for 1 day results in activities of 130-140 U/l |
| 1.1.3.15 | (S)-2-hydroxy-acid oxidase |
synthesis |
coexpression of N-demethylase NdmB gene from Pseudomonas putida CBB5 and glycolate oxidase gene in Escherichia coli. By two-step purification of Ni affinity chromatography and Q-Sepharose chromatography, the coexpressed NdmB and GO are separated and result in a 15.8fold purification with 8.7% yield and 12.8fold purification with 7.2% yield, respectively |
| 1.1.99.B9 | (S)-2-hydroxycarboxylate dehydrogenase |
synthesis |
coupling of asymmetric oxidation of racemic 2-hydroxyacids with the opposite stereoselective reduction of 2-ketoacids for the stereoselective oxidoreductive deracemization to (R)-2-hydroxyacids, using a one-pot biocatalysis by resting cells of Saccharomyces cerevisiae strain ZJB5074 and Pseudomonas aeruginosa CCTCC M 2011394. Substituted racemic hydroxy(phenyl)acetic acids are converted to (R)-2-hydroxy-2-phenyl acetic acids with 55-98% conversion rate and 99.9% enantiomeric excess |
| 1.1.99.B9 | (S)-2-hydroxycarboxylate dehydrogenase |
synthesis |
enzyme can be used for the concurrent obtaining of aromatic (R)-2-hydroxyacids and aromatic 2-ketoacids by oxidation of aromatic 2-hydroxyacids in one-step biotransformation |
| 1.1.1.280 | (S)-3-hydroxyacid-ester dehydrogenase |
synthesis |
ethyl (2R,3S)-3-hydroxy-2-methylbutanoate is a useful starting material for the synthesis of ferroelectric liquid crystal compounds and various other biologically active substances |
| 1.1.1.254 | (S)-carnitine 3-dehydrogenase |
synthesis |
Agrobacterium radiobacter can be used for conversion of the waste product L(-)-carnitine to poly-beta-hydroxybutyrate valuable as a biodegradable and biocompatible plastic |
| 1.14.19.65 | (S)-cheilanthifoline synthase |
synthesis |
a microbial system is established for producing a protoberberine-type alkaloid (stylopine) in Pichia cells |
